Triple Helix Structure

World's First
Regenerative Human Collagen

Engineered using our patented in vitro tissue regeneration technology — a 100% human-derived collagen matrix that closely mirrors the architecture and function of the body's own tissue. Not recombinant. Not animal-derived. Genuinely human.

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REGENERATED HUMAN COLLAGEN INTACT TRIPLE HELIX STRUCTURE NO IMMUNO- GENICITY BATCH-TO-BATCH STABILITY TYPE I COLLAGEN CHAIN LENGTH PURITY NO CYTO- TOXICITY
Intact Triple Helix Structure
The hallmark of native collagen — a right-handed triple helix of three polypeptide α-chains — is fully preserved. This intact architecture is the prerequisite for proper cell–receptor binding, mechanical resilience, and bioactive signalling.
No Immunogenicity
Human-homologous design means the immune system recognises this collagen as structurally "self" — dramatically reducing immune reactivity, calcification, and chronic inflammatory response.
Batch-to-Batch Stability
Controlled in vitro cellular expression delivers reproducible structural characteristics across every lot — eliminating variability and ensuring predictable, consistent clinical outcomes.
Type I Collagen Chain Length
Authentic human fibroblasts produce Type I/III collagen with full-sequence active gene sites and precise α-chain lengths — preserving structural integrity lost in conventional extraction or recombinant systems.
Exceptional Molecular Purity
Advanced GMP-aligned purification ensures freedom from residual cellular debris, endotoxins, and non-collagenous protein contaminants — protecting both safety profiles and formulation stability.
No Cytotoxicity
100% human-derived collagen eliminates cytotoxic contamination and zoonotic transmission risks inherent to bovine, porcine, and marine processing. GMP-aligned from seed cell to final lot.

Produced through tissue engineering and in vitro cellular expression techniques, our regenerated human collagen cultivates authentic human cells that produce the exact structural characteristics and biological functions of the body's native collagen — including Type I/III collagen with full-sequence active gene sites and precise chain lengths.

Human Skin Tissue Laboratory

Intact Triple-Helix
Confirmed

CD Spectroscopy SDS-PAGE
Circular Dichroism
SDS-PAGE

Signature CD profile confirms a perfectly folded native triple-helix — optical activity bands consistent with natural human Type I collagen.

Negative Band 198 nm  −33.71 mdeg
Positive Band 221.5 nm  +3.21 mdeg
Interpretation Native Helix — Confirmed

Distinct α1 and α2 bands align precisely with native human collagen molecular weight — validating full-length polypeptide chains and structural fidelity.

α1
~116 kDa
α2
~97 kDa

Matches native human collagen molecular weight — precisely.

Four-Level Fibrillar Architecture

AMINO ACID SEQUENCE

Full-sequence active gene sites preserved — our human cells express collagen with the complete, authentic amino acid sequence of natural Type I collagen, including the Gly-X-Y repeat motif essential for triple-helix assembly. No truncation. No synthetic shortcuts.

Amino Acid Sequence Triple-Helix Conformation Fibril Formation Extracellular Matrix Network